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• W2023289678 abstract "The effect of heat on the conformation of arachin at pH 3.6 has been investigated by the techniques of viscosity, u.v. difference spectroscopy, fluorescence spectroscopy, spectrophotometric titration of tyrosine, and near and far u.v. circular dichroism. An increase in intrinsic viscosity, a blue shift in the u.v. absorption spectrum, an increase in the number of titratable tyrosines and some loss of both tertiary and secondary structures were observed in arachin at pH 3.6. After heating the protein at this pH the protein denaturation is enhanced, although it did not go to completion. These observations suggested that denaturation is a possible intermediate step involved in the heat-induced protein—protein interactions that lead to gelation of arachin at pH 3.6." @default.
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• W2023289678 date "1987-04-01" @default.
• W2023289678 modified "2023-09-27" @default.
• W2023289678 title "Heat-induced conformational changes in arachin at low pH: mechanism of gel formation" @default.
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• W2023289678 doi "https://doi.org/10.1016/s0268-005x(87)80001-2" @default.
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